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7PD9

Crystal structure of CD73 in complex with riboflavin in the open form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002953molecular_function5'-deoxynucleotidase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006196biological_processAMP catabolic process
A0006259biological_processDNA metabolic process
A0007159biological_processleukocyte cell-cell adhesion
A0008252molecular_functionnucleotidase activity
A0008253molecular_function5'-nucleotidase activity
A0008270molecular_functionzinc ion binding
A0009166biological_processnucleotide catabolic process
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010035biological_processobsolete response to inorganic substance
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0033198biological_processresponse to ATP
A0042802molecular_functionidentical protein binding
A0046032biological_processADP catabolic process
A0046034biological_processATP metabolic process
A0046086biological_processadenosine biosynthetic process
A0046872molecular_functionmetal ion binding
A0050340molecular_functionthymidylate 5'-phosphatase activity
A0050483molecular_functionIMP 5'-nucleotidase activity
A0050484molecular_functionGMP 5'-nucleotidase activity
A0050728biological_processnegative regulation of inflammatory response
A0055074biological_processcalcium ion homeostasis
A0070062cellular_componentextracellular exosome
A0098552cellular_componentside of membrane
A0106411molecular_functionXMP 5'-nucleosidase activity
A0110148biological_processobsolete biomineralization
A0140928biological_processinhibition of non-skeletal tissue mineralization
Functional Information from PROSITE/UniProt
site_idPS00785
Number of Residues13
Details5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. LtILHTnDvHSrL
ChainResidueDetails
ALEU29-LEU41

site_idPS00786
Number of Residues12
Details5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaLGNHEFD
ChainResidueDetails
ATYR110-ASP121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22997138, ECO:0000269|PubMed:23142347, ECO:0000269|PubMed:34403084, ECO:0007744|PDB:4H1S, ECO:0007744|PDB:7P9N
ChainResidueDetails
AASP36

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22997138, ECO:0000269|PubMed:23142347, ECO:0000269|PubMed:34403084, ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I, ECO:0007744|PDB:7P9N
ChainResidueDetails
AHIS38

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22997138, ECO:0000269|PubMed:23142347, ECO:0000269|PubMed:34403084, ECO:0007744|PDB:4H1S, ECO:0007744|PDB:4H1Y, ECO:0007744|PDB:4H2B, ECO:0007744|PDB:4H2F, ECO:0007744|PDB:4H2G, ECO:0007744|PDB:4H2I, ECO:0007744|PDB:7P9N
ChainResidueDetails
AASP85
AASN117
AHIS220
AHIS243

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:34403084, ECO:0007744|PDB:7PBA
ChainResidueDetails
AARG354
AASN390
AARG395
APHE417
APHE500
AASP506

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:23142347
ChainResidueDetails
AHIS118

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:23142347
ChainResidueDetails
AASP121

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:2129526
ChainResidueDetails
ASER549

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP53

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22997138, ECO:0000269|PubMed:23142347
ChainResidueDetails
AASP311

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASP333

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASP403

227111

PDB entries from 2024-11-06

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